{"title":"Exploration of Myosin Heavy Chain Fragments within the Protein Network in Disintegrated Deep-Sea Bonefish Pterothrissus gissu Surimi Gel","authors":"Yuri Kominami*, Ryoko Nakamizo, Yoko Matsuoka, Nobuhiko Ueki, Jianrong Wan, Shugo Watabe and Hideki Ushio, ","doi":"10.1021/acsfoodscitech.4c0088010.1021/acsfoodscitech.4c00880","DOIUrl":"https://doi.org/10.1021/acsfoodscitech.4c00880https://doi.org/10.1021/acsfoodscitech.4c00880","url":null,"abstract":"<p >A significant challenge in the surimi industry is the softening of surimi gel caused by proteolytic degradation of myosin heavy chain (MHC) during heating. Details of MHC fragmentation remain unclear despite being crucial to understanding the mechanism of surimi gel softening. This study employed in-gel digestion coupled with mass spectrometric analysis (GeLC–MS/MS) of the urea-soluble proteins from surimi gels from deep-sea bonefish <i>Pterothrissus gissu</i> to explore myosin heavy chain fragments within the protein network. More MHC fragments of ∼28, 48, 70, 150, and 190 kDa were found in softer <i>P. gissu</i> surimi gels. The results of the sequence mapping indicate that ∼150 and 190 kDa MHC fragments were generated by cleavage at the light meromyosin (LMM) region. The results of the present study, combined with our previous findings, suggest a differential distribution of MHC fragments in the disintegrated <i>P. gissu</i> surimi gel based on their size. Specifically, longer MHC fragments exist in the protein network, while shorter fragments (∼28, 48, and 70 kDa) and peptides derived from the LMM region are partially soluble in water.</p>","PeriodicalId":72048,"journal":{"name":"ACS food science & technology","volume":"5 3","pages":"1072–1081 1072–1081"},"PeriodicalIF":2.6,"publicationDate":"2025-02-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143667021","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Novel Formulations of Cinnamon- and Orange-Flavored Synbiotic Corn Chocolates with Enhanced Functional Properties and Probiotic Survival Rates","authors":"Shubhi Singh, and , Smriti Gaur*, ","doi":"10.1021/acsfoodscitech.4c0074110.1021/acsfoodscitech.4c00741","DOIUrl":"https://doi.org/10.1021/acsfoodscitech.4c00741https://doi.org/10.1021/acsfoodscitech.4c00741","url":null,"abstract":"<p >This study aimed to develop synbiotic chocolates using <i>Lactobacillus acidophilus</i> La-14 and <i>Lactobacillus rhamnosus</i> GG as probiotic sources and corn, honey, cinnamon, and orange as natural prebiotic and flavoring agents. Chocolates were evaluated for moisture, pH, protein, fat, antioxidant, flavonoid, and phenolic content. According to one-way analysis of variance, sample 4 containing <i>L. rhamnosus</i> GG, corn, honey, and orange exhibited highest protein content (8.06%) as well as antioxidant activity (139.54 mg of ascorbic acid equivalent/100 g) when compared to control samples. Physicochemical analysis indicated reduction in crystallinity ratio (39.90%–48.60%) in synbiotic chocolates compared to control (57.48%). Synbiotic chocolates also enhanced probiotic viability when exposed to simulated gastrointestinal conditions and maintained cell counts above 5 log colony forming units/g for up to 125 days under storage. Hence, findings demonstrate the potential of natural prebiotic ingredients to develop synbiotic chocolates with desirable qualities, therefore offering avenues in the functional food domain.</p>","PeriodicalId":72048,"journal":{"name":"ACS food science & technology","volume":"5 4","pages":"1268–1279 1268–1279"},"PeriodicalIF":2.6,"publicationDate":"2025-02-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143842302","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Ixchel G. Moreno-Vallejo, Perla J. Gudiño-Ramírez, María Elena Sosa-Morales, María Hernández-Carrión, Aureliano Rodríguez-Cortina, Paulo C. B. Campagnol and Julián Andrés Gómez-Salazar*,
{"title":"Lipid Profile and Physicochemical Properties of Chorizo with Partial Replacement of Encapsulated Sacha Inchi Oil","authors":"Ixchel G. Moreno-Vallejo, Perla J. Gudiño-Ramírez, María Elena Sosa-Morales, María Hernández-Carrión, Aureliano Rodríguez-Cortina, Paulo C. B. Campagnol and Julián Andrés Gómez-Salazar*, ","doi":"10.1021/acsfoodscitech.4c0038210.1021/acsfoodscitech.4c00382","DOIUrl":"https://doi.org/10.1021/acsfoodscitech.4c00382https://doi.org/10.1021/acsfoodscitech.4c00382","url":null,"abstract":"<p >Fresh chorizos were produced by replacing 3 and 6% of their animal fat content with microparticles of sacha inchi-encapsulated oil (SIEO) produced by spray drying. The effect of this lipid reformulation on fresh chorizos’ physicochemical, oxidative, and lipid indices (atherogenic index and thrombogenic index) was assessed. The moisture content, water activity, and pH values of the chorizos were not influenced by the replacement of fat (<i>p</i> > 0.05). The replacement of 3 and 6% animal fat by SIEO reduced the fat content and increased the levels of <i>n</i>–3/<i>n</i>–6 ratios and polyunsaturated fraction by 14.8 and 32.2%, respectively. The kinetics of oxidation and hardness of chorizo during storage were adequately adjusted to a first-order model. The addition of SIEO slightly increased lipid oxidation and hardness in the chorizo samples. SIEO is a good alternative in partially replacing pork fat without significantly affecting the physicochemical properties but improving its fatty acid profile.</p>","PeriodicalId":72048,"journal":{"name":"ACS food science & technology","volume":"5 3","pages":"972–980 972–980"},"PeriodicalIF":2.6,"publicationDate":"2025-02-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143667014","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Vignaesh Dhanabalan, K. A. Martin Xavier*, Kasturi Chattopadhyay, Kurukkan Kunnath Asha, Amjad K. Balange, L. N. Murthy and Binaya Bhushan Nayak,
{"title":"Effect of the Type of Enzyme and Degree of Hydrolysis on the Antioxidant Properties of Paste Shrimp Protein Hydrolysates Prepared by Varying in Vitro Enzymatic Process","authors":"Vignaesh Dhanabalan, K. A. Martin Xavier*, Kasturi Chattopadhyay, Kurukkan Kunnath Asha, Amjad K. Balange, L. N. Murthy and Binaya Bhushan Nayak, ","doi":"10.1021/acsfoodscitech.4c0092210.1021/acsfoodscitech.4c00922","DOIUrl":"https://doi.org/10.1021/acsfoodscitech.4c00922https://doi.org/10.1021/acsfoodscitech.4c00922","url":null,"abstract":"<p >Protein hydrolysates from Paste Shrimp (<i>Acetes</i> spp.) were produced using four commercial proteolytic enzymes (alcalase, papain, trypsin, and pepsin) independently. The degree of hydrolysis (DH) from 5 to 30% was standardized using a linear regression plot viz. DH (%) against the duration of hydrolysis (min). In the present study, the influence of DH on antioxidant and antihypertensive properties, such as 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activity, 2 2′-azino-bis-3-ethylbenzothiazoline sulfonic acid (ABTS) radical scavenging activity, metal chelating activity, and angiotensin converting enzyme (ACE) inhibition activity, was investigated. Papain-mediated hydrolysate displayed the highest DPPH radical scavenging activity while trypsin-mediated hydrolysate showed the highest ABTS radical scavenging activity at 30% DH. The highest metal chelating activity was obtained at 20% DH in alcalase mediated hydrolysate. The highest ACE inhibiting activity was detected in Alcalase-mediated hydrolysates at 30% DH, and the activity increased with rising DH. This study revealed that the increase in the extent of hydrolysis with a suitable enzyme can significantly enhance the bioactive properties of the <i>Acetes</i> protein hydrolysate.</p>","PeriodicalId":72048,"journal":{"name":"ACS food science & technology","volume":"5 3","pages":"1124–1131 1124–1131"},"PeriodicalIF":2.6,"publicationDate":"2025-02-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143666941","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Jairo Andrés CamañoEchavarría*, Rachel Irankunda, Philippe Arnoux, Christelle Mathé, Jean-Michel Girardet, Céline Cakir-Kiefer, Arnaud Risler, Loïc Stefan, Cédric Paris, José Edgar Zapata Montoya, Katalin Selmeczi and Laetitia Canabady-Rochelle*,
{"title":"Characterization and Bioactivities of Gelatin Hydrolysates of Red Tilapia (Oreochromis spp.) Scale Byproducts","authors":"Jairo Andrés CamañoEchavarría*, Rachel Irankunda, Philippe Arnoux, Christelle Mathé, Jean-Michel Girardet, Céline Cakir-Kiefer, Arnaud Risler, Loïc Stefan, Cédric Paris, José Edgar Zapata Montoya, Katalin Selmeczi and Laetitia Canabady-Rochelle*, ","doi":"10.1021/acsfoodscitech.4c0091810.1021/acsfoodscitech.4c00918","DOIUrl":"https://doi.org/10.1021/acsfoodscitech.4c00918https://doi.org/10.1021/acsfoodscitech.4c00918","url":null,"abstract":"<p >This study explores the production of gelatin hydrolysates with metal-chelating peptides derived from red tilapia scales and investigates their biofunctional properties. Gelatin was enzymatically hydrolyzed using Alcalase (Alc-GH), Flavourzyme (Flav-GH), or a sequential combination of Alcalase and Flavourzyme (Alc+Flav-GH). Alc-GH and Alc+Flav-GH were ultrafiltrated at 1 kDa cutoff. Alc+Flav-GH, characterized by a high proportion of small-sized peptides, exhibited superior metal-chelating ability, as determined by switchSENSE and was associated with enhanced antioxidant activity. Ultrafiltration improved the Fe<sup>2+</sup>-chelating properties of both fractions compared to their respective whole hydrolysates. All of the hydrolysates and their ultrafiltrates showed remarkable ACE inhibitory activity. Specifically, the ≤1 kDa Alc-GH fraction produced small-sized Fe<sup>2+</sup>-chelating peptides with ACE inhibitory activity, whereas the ≤1 kDa Alc+Flav-GH fraction efficiently generated Ni<sup>2+</sup>-chelating peptides with strong antioxidant potential. LC-MS/MS data showed peptides rich in Asp, Glu, Ser, Lys, and Arg, which may contribute to their metal-chelating and antioxidant properties.</p>","PeriodicalId":72048,"journal":{"name":"ACS food science & technology","volume":"5 3","pages":"1100–1115 1100–1115"},"PeriodicalIF":2.6,"publicationDate":"2025-02-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143666942","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Ádina L. Santana, Jaymi Peterson, Ramasamy Perumal, Yong Hoon Joo, Seoung-Ho Lee, Kaliramesh Siliveru and Dmitriy Smolensky*,
{"title":"High-Molecular-Weight Polyphenols from Sorghum Bicolor Retain Higher Glycation Inhibition and Cancer Cell Inhibition In vitro Compared to Small-Molecular-Weight Polyphenols after Separation Using Sephadex LH-20","authors":"Ádina L. Santana, Jaymi Peterson, Ramasamy Perumal, Yong Hoon Joo, Seoung-Ho Lee, Kaliramesh Siliveru and Dmitriy Smolensky*, ","doi":"10.1021/acsfoodscitech.4c0085110.1021/acsfoodscitech.4c00851","DOIUrl":"https://doi.org/10.1021/acsfoodscitech.4c00851https://doi.org/10.1021/acsfoodscitech.4c00851","url":null,"abstract":"<p >Sorghum contains a diverse array of phenolic compounds, including condensed tannins, phenolic acids, and 3-deoxyanthocyanidins. The differences in bioactivity among these phenolics are not well studied. This work improved existing methods to selectively separate polyphenols based on size using extracts of highly phenolic sorghum varieties. Sephadex LH-20 resin was used to separate large-molecular-weight condensed tannins from oligomeric and monomeric polyphenols. Flavonoid monomers, including 3-deoxyanthocyanidins, were highly concentrated in ethanolic fractions, while the large polyphenol polymers were concentrated in acetone fractions. The bioactivity of separated fractions was evaluated via glycation inhibition and colorectal cancer cell inhibition (HCT116 and RKO). The results demonstrated that high- molecular-weight fractions demonstrated significantly higher (<i>p</i> < 0.05) bioactivity than low- molecular-weight fractions in both assays. This work provides valuable information on the separation of sorghum polyphenols by size and their bioactivity.</p>","PeriodicalId":72048,"journal":{"name":"ACS food science & technology","volume":"5 3","pages":"1010–1023 1010–1023"},"PeriodicalIF":2.6,"publicationDate":"2025-02-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://pubs.acs.org/doi/epdf/10.1021/acsfoodscitech.4c00851","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143666913","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Gabriela R. Tapia-Álvarez, Élida Gastélum-Martínez, Neith Pacheco, Lía S. Valencia-Chan, Rosa E. Moo-Puc, Jorge M. Santamaría-Fernández, Inocencio Higuera-Ciapara, Karlina García-Sosa and Luis M. Peña-Rodríguez*,
{"title":"Characterization of the Caimito Fruit (Chrysophyllum cainito L.) as a Promising Functional Food","authors":"Gabriela R. Tapia-Álvarez, Élida Gastélum-Martínez, Neith Pacheco, Lía S. Valencia-Chan, Rosa E. Moo-Puc, Jorge M. Santamaría-Fernández, Inocencio Higuera-Ciapara, Karlina García-Sosa and Luis M. Peña-Rodríguez*, ","doi":"10.1021/acsfoodscitech.4c0091510.1021/acsfoodscitech.4c00915","DOIUrl":"https://doi.org/10.1021/acsfoodscitech.4c00915https://doi.org/10.1021/acsfoodscitech.4c00915","url":null,"abstract":"<p >The global demographic transformation, marked by declining birth rates and increased life expectancy, is motivating researchers to seek foods that can alleviate oxidative stress, a major factor linked to aging and chronic diseases. This study evaluated the caimito fruit (<i>Chrysophyllum cainito</i>), traditionally consumed in Yucatán, Mexico, as a functional food through detailed characterization protocols. For the first time, this work establishes a maturity index value and provides standard parameters useful when developing caimito-derived products. The phenolic content in the caimito pulp was comparable to that of fresh strawberries and correlated with its protective capacity against H<sub>2</sub>O<sub>2</sub>-induced oxidative stress in K562 cells. UPLC–MS analysis tentatively identified <i>C</i>-glucosides of luteolin and 3-<i>O</i>-glycosides of myricetin and quercetin, known for their antioxidant properties, as the main phenolic components. These findings support the functional potential of caimito, suggesting that incorporating this uniquely flavored fruit into a balanced diet may help reduce oxidative stress and improve health.</p>","PeriodicalId":72048,"journal":{"name":"ACS food science & technology","volume":"5 3","pages":"1091–1099 1091–1099"},"PeriodicalIF":2.6,"publicationDate":"2025-02-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143666912","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Elif Gokcen Ates, Gokcem Tonyali Karsli, Hami Alpas, Emin Burçin Ozvural and Mecit H. Oztop*,
{"title":"Effects of High Hydrostatic Pressure (HHP) on the Extraction and Functional Characteristics of Chickpea Proteins and Saponins","authors":"Elif Gokcen Ates, Gokcem Tonyali Karsli, Hami Alpas, Emin Burçin Ozvural and Mecit H. Oztop*, ","doi":"10.1021/acsfoodscitech.4c0097510.1021/acsfoodscitech.4c00975","DOIUrl":"https://doi.org/10.1021/acsfoodscitech.4c00975https://doi.org/10.1021/acsfoodscitech.4c00975","url":null,"abstract":"<p >This study investigated the influence of High Hydrostatic Pressure (HHP) on the extraction of proteins and saponins from chickpeas, as well as its effects on their functional properties. HHP was applied at two pressure levels (200 and 400 MPa) at 40 °C for 5 min and compared with conventional heating (90 °C for 5 min, no pressure). The results showed that HHP significantly improved the extraction of soluble proteins and saponins, especially at 200 MPa. At higher pressure (400 MPa), there was a slight decrease in extraction due to the possible formation of protein aggregates. The study also found that HHP-treated samples had better foaming and emulsifying abilities, which are important for food applications. Emulsions produced under HHP were more stable than those from the control treatment. Overall, HHP proved to be an effective method for improving both the extraction and functionality of chickpea bioactives, with potential applications in food.</p>","PeriodicalId":72048,"journal":{"name":"ACS food science & technology","volume":"5 3","pages":"1116–1123 1116–1123"},"PeriodicalIF":2.6,"publicationDate":"2025-02-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143666866","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Carotenes from Pumpkin Flesh and Peel: A Review on Their Physicochemical Properties, Preparation Techniques, Detection Methods and Antioxidant Potential","authors":"Hailang Ge, Lingli Yang, Qiqi Yao, Yingxuan Gu, Chenxu Zhang, Xuyang Liu, Fen Huang and Yongjun Zhang*, ","doi":"10.1021/acsfoodscitech.4c0096410.1021/acsfoodscitech.4c00964","DOIUrl":"https://doi.org/10.1021/acsfoodscitech.4c00964https://doi.org/10.1021/acsfoodscitech.4c00964","url":null,"abstract":"<p >The pumpkin, an annual trailing herbaceous plant belonging to the Cucurbitaceae family and the <i>Cucurbita</i> genus, has a long cultivation history and possesses strong regenerative ability, high adaptability, and high yield. It is an economically important species cultivated worldwide. The pumpkin flesh and peel contain pumpkin pigments, which are rare natural pigments with strong coloring power. They overcome the disadvantages of natural pigments having weaker coloring power than synthetic pigments and have a wide range of applications. The main components of pumpkin pigments include α-carotene, β-carotene, lutein, and zeaxanthin, which have high nutritional value. The paper reviews the physical and chemical properties of pumpkin flesh and peel pigments, preparation techniques (conventional and current technologies), detection methods, and antioxidant potential (including free radical scavenging ability, antilipid oxidation ability, and antioxidative stress ability) with the aim of providing references for the application of pumpkin pigments in the food, cosmetics, and pharmaceutical industries.</p>","PeriodicalId":72048,"journal":{"name":"ACS food science & technology","volume":"5 3","pages":"898–908 898–908"},"PeriodicalIF":2.6,"publicationDate":"2025-02-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143666864","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Functions of Salted Duck Egg White in Surimi Gel Formation during Two-Step Heating as Hen Egg White Substitutes","authors":"Prim Srisai, and , Kanokrat Limpisophon*, ","doi":"10.1021/acsfoodscitech.4c0074310.1021/acsfoodscitech.4c00743","DOIUrl":"https://doi.org/10.1021/acsfoodscitech.4c00743https://doi.org/10.1021/acsfoodscitech.4c00743","url":null,"abstract":"<p >This study explores salted duck egg white (SDEW) as a protease inhibitor and gel enhancer in surimi, comparing its efficacy with hen egg white powders. SDEW exhibited superior trypsin inhibition (53–54%) than hen egg white powders (37–49%), likely due to ovomucoid, ovoinhibitor, and duck ovostatin. During two-step heating, at 40 °C preincubation, storage modulus (<i>G</i>′) declined, but at trypsin activity of 50–60 °C, SDEW-powder achieved the highest <i>G</i>′ values. The low TCA-soluble peptide content (1.48–1.52 μmol tyrosine g<sup>–1</sup>) in surimi with SDEW confirmed protease inhibition, comparable to commercial hen egg white powder (CHEP). Above 70 °C, SDEW improved gel elasticity, disulfide bond formation, and water entrapment (13–15% expressible moisture), achieving gel strength of 630–665 g cm, surpassing CHEP (524 g cm), and approaching premium-grade surimi (>600 g cm). Microstructural analysis revealed a denser gel network, highlighting SDEW-powder as a viable hen egg white substitute for surimi gelation and quality enhancement.</p>","PeriodicalId":72048,"journal":{"name":"ACS food science & technology","volume":"5 3","pages":"981–990 981–990"},"PeriodicalIF":2.6,"publicationDate":"2025-02-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://pubs.acs.org/doi/epdf/10.1021/acsfoodscitech.4c00743","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143666861","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}